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Literature summary extracted from

  • Verhaeghe, T.; Diricks, M.; Aerts, D.; Soetaert, W.; Desmet, T.
    Mapping the acceptor site of sucrose phosphorylase from Bifidobacterium adolescentis by alanine scanning (2013), J. Mol. Catal. B, 96, 81-88.
No PubMed abstract available

Application

EC Number Application Comment Organism
2.4.1.7 synthesis sucrose phosphorylase is a promising biocatalyst for the production of special sugars and glycoconjugates, but its transglycosylation activity rarely exceeds the competing hydrolytic reaction Bifidobacterium adolescentis

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.7 D342A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 H234A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 L343A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 P134A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 Q345A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 R135A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 Y132A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 Y196A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis
2.4.1.7 Y344A saturation mutagensis, transglucosylation and hydrolytic side activity of the mutant compared to the wild-type Bifidobacterium adolescentis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.7 sucrose + phosphate Bifidobacterium adolescentis
-
D-fructose + alpha-D-glucose 1-phosphate
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.7 Bifidobacterium adolescentis Q84HQ2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.7 sucrose + D-arabitol
-
Bifidobacterium adolescentis pyridoxine + alpha-D-glucose 1-phosphate
-
r
2.4.1.7 sucrose + phosphate
-
Bifidobacterium adolescentis D-fructose + alpha-D-glucose 1-phosphate
-
r

General Information

EC Number General Information Comment Organism
2.4.1.7 additional information mapping of the acceptor site of the enzyme by saturation mutagenesis and screening, overview. Residues Arg135, Leu343, and Tyr344 contribute to the specificity for phosphate, residues Tyr132 and Asp342 contribute to the specificity for D-fructose, and residues Pro134, Tyr196, His234, Gln345 contribute to the specificity for both. Alternative acceptors that are glycosylated rather efficiently (e.g. D-arabitol) interact with the same residues as fructose, whereas poor acceptors like pyridoxine do not seem to make any specific interactions with the enzyme Bifidobacterium adolescentis